ID PUR8_SYNY3 Reviewed; 431 AA. AC P74384; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 02-SEP-2026, entry version 153. DE RecName: Full=Adenylosuccinate lyase; DE Short=ASL; DE EC=4.3.2.2 {ECO:0000250|UniProtKB:P0AB89}; DE AltName: Full=Adenylosuccinase; DE Short=ASase; GN Name=purB; OrderedLocusNames=sll0421; OS Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Merismopediaceae; Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27184 / PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). CC -!- FUNCTION: Catalyzes two reactions in de novo purine nucleotide CC biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N- CC succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta- CC D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4- CC carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D- CC ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate CC (ADS or N(6)-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP) CC and fumarate. {ECO:0000250|UniProtKB:P0AB89}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(6)-(1,2-dicarboxyethyl)-AMP = fumarate + AMP; CC Xref=Rhea:RHEA:16853, ChEBI:CHEBI:29806, ChEBI:CHEBI:57567, CC ChEBI:CHEBI:456215; EC=4.3.2.2; CC Evidence={ECO:0000250|UniProtKB:P0AB89}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16854; CC Evidence={ECO:0000250|UniProtKB:P0AB89}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4- CC carboxamido]succinate = 5-amino-1-(5-phospho-beta-D- CC ribosyl)imidazole-4-carboxamide + fumarate; Xref=Rhea:RHEA:23920, CC ChEBI:CHEBI:29806, ChEBI:CHEBI:58443, ChEBI:CHEBI:58475; EC=4.3.2.2; CC Evidence={ECO:0000250|UniProtKB:P0AB89}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23921; CC Evidence={ECO:0000250|UniProtKB:P0AB89}; CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP CC from IMP: step 2/2. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5- CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5- CC phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2. CC -!- SUBUNIT: Homooligomer. Residues from neighboring subunits contribute CC catalytic and substrate-binding residues to each active site (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000022; BAA18481.1; -; Genomic_DNA. DR PIR; S76222; S76222. DR AlphaFoldDB; P74384; -. DR SMR; P74384; -. DR FunCoup; P74384; 469. DR IntAct; P74384; 1. DR STRING; 1148.gene:10499362; -. DR PaxDb; 1148-gene:10499362; -. DR EnsemblBacteria; BAA18481; BAA18481; BAA18481. DR KEGG; syn:sll0421; -. DR eggNOG; COG0015; Bacteria. DR InParanoid; P74384; -. DR PhylomeDB; P74384; -. DR UniPathway; UPA00074; UER00132. DR UniPathway; UPA00075; UER00336. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity; ISS:UniProtKB. DR GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; ISS:UniProtKB. DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006163; P:purine nucleotide metabolic process; IBA:GO_Central. DR CDD; cd01360; Adenylsuccinate_lyase_1; 1. DR FunFam; 1.10.275.10:FF:000006; Adenylosuccinate lyase; 1. DR FunFam; 1.10.40.30:FF:000007; Adenylosuccinate lyase; 1. DR FunFam; 1.20.200.10:FF:000008; Adenylosuccinate lyase; 1. DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1. DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1. DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1. DR InterPro; IPR019468; AdenyloSucc_lyase_C. DR InterPro; IPR024083; Fumarase/histidase_N. DR InterPro; IPR020557; Fumarate_lyase_CS. DR InterPro; IPR000362; Fumarate_lyase_fam. DR InterPro; IPR022761; Fumarate_lyase_N. DR InterPro; IPR008948; L-Aspartase-like. DR InterPro; IPR004769; Pur_lyase. DR NCBIfam; TIGR00928; purB; 1. DR PANTHER; PTHR43172; ADENYLOSUCCINATE LYASE; 1. DR PANTHER; PTHR43172:SF1; ADENYLOSUCCINATE LYASE; 1. DR Pfam; PF10397; ADSL_C; 1. DR Pfam; PF00206; Lyase_1; 1. DR PRINTS; PR00145; ARGSUCLYASE. DR PRINTS; PR00149; FUMRATELYASE. DR SMART; SM00998; ADSL_C; 1. DR SUPFAM; SSF48557; L-aspartase-like; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. PE 3: Inferred from homology; KW Lyase; Purine biosynthesis; Reference proteome. FT CHAIN 1..431 FT /note="Adenylosuccinate lyase" FT /id="PRO_0000137885" FT ACT_SITE 141 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:P0AB89" FT ACT_SITE 262 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:P0AB89" FT BINDING 4..5 FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP" FT /ligand_id="ChEBI:CHEBI:57567" FT /evidence="ECO:0000250|UniProtKB:P0AB89" FT BINDING 67..69 FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP" FT /ligand_id="ChEBI:CHEBI:57567" FT /evidence="ECO:0000250|UniProtKB:P0AB89" FT BINDING 93..94 FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP" FT /ligand_id="ChEBI:CHEBI:57567" FT /evidence="ECO:0000250|UniProtKB:P0AB89" FT BINDING 212 FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP" FT /ligand_id="ChEBI:CHEBI:57567" FT /evidence="ECO:0000250|UniProtKB:P0AB89" FT BINDING 263 FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP" FT /ligand_id="ChEBI:CHEBI:57567" FT /evidence="ECO:0000250|UniProtKB:P0AB89" FT BINDING 268..270 FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP" FT /ligand_id="ChEBI:CHEBI:57567" FT /evidence="ECO:0000250|UniProtKB:P0AB89" FT BINDING 307..311 FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP" FT /ligand_id="ChEBI:CHEBI:57567" FT /evidence="ECO:0000250|UniProtKB:P0AB89" SQ SEQUENCE 431 AA; 48420 MW; 38811A661A62BD07 CRC64; MIERYTLPEM GKIWTDTYKL QTWLDVEIAV CEAQAELGYI PQAAVDEIKA KAKFDPQRVL EIEAEVRHDV IAFLTNVNEY VGDAGRYIHL GLTSSDVLDT ALALQLVASL DLILEQLEKL IQAIRYQAQQ HRYTVMVGRS HGIHAEPITF GFKLAGWLAE VLRNRDRLVR VAQSIAVGKI SGAVGTYANI DPKVEAIACQ KLGLEPDTAS TQVISRDRHA EYVQQLALLA ASLERFAVEI RNLQRTDVLE VEEYFSKGQK GSSAMPHKRN PIRSERLTGM ARLVRGHAVA ALENVALWHE RDISHSSVER VAFPDCCILT HFMLKETTDL VKNLLVYPEN MKRNMNVYGG VIFSQKVLLA LVEKGMNRED AYRVVQGSAH QAWNTEGGNF EELVRADAQV TALLSAEEID QCFDPQQHLT NLAEIYSRLD I //